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. 2017 Apr 4;7:603. doi: 10.1038/s41598-017-00703-w

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Comparison of LC-MS/MS and MALDI MSI data: the agreement between the fold-changes determined by LC-MS/MS of microdissected regions (microdissected regions are indicated in top histological image) and MSI datasets is demonstrated for three protein ions. In each case the LC-MS/MS relative quantification confirmed that observed with MALDI MSI. (a) Images extracted from the MSI dataset for 60 S ribosomal protein L38, High mobility group protein, 60 S ribosomal protein L34 (from the top). (b) LC-MS/MS relative quantification: the bar charts report the sum of the areas of each protein’s tryptic peptides (data are mean area ± standard deviation).